Differential activation of mitogen-activated protein kinase signalling pathways in the hippocampus of CRND8 transgenic mouse, a model of Alzheimer's disease

Neuroscience ◽  
2008 ◽  
Vol 153 (3) ◽  
pp. 618-633 ◽  
Author(s):  
M.G. Giovannini ◽  
F. Cerbai ◽  
A. Bellucci ◽  
C. Melani ◽  
C. Grossi ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Kinase ◽  
Transgenic Mouse ◽  
Mitogen Activated Protein Kinase ◽  
Signalling Pathways ◽  
Differential Activation ◽  
Model Of Alzheimer’S Disease ◽  
Mitogen Activated Protein ◽  
Protein Kinase Signalling

Plant mitogen-activated protein kinase signalling pathways in the limelight

2000 ◽  
pp. 299-354 ◽  
Author(s):  
S Jouannic ◽  
A.-S Leprince ◽  
A Hamal ◽  
A Picaud ◽  
M Kreis ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Signalling Pathways ◽  
Mitogen Activated Protein ◽  
Protein Kinase Signalling

scholarly journals Increased tau Phosphorylation on Mitogen-Activated Protein Kinase Consensus Sites and Cognitive Decline in Transgenic Models for Alzheimer's Disease and FTDP-17: Evidence for Distinct Molecular Processes Underlying tau Abnormalities

2005 ◽  
Vol 25 (1) ◽  
pp. 278-293 ◽  
Author(s):  
Sarah L. Lambourne ◽  
Lynda A. Sellers ◽  
Toby G. Bush ◽  
Shewly K. Choudhury ◽  
Piers C. Emson ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Kinase ◽  
Tau Phosphorylation ◽  
Mitogen Activated Protein Kinase ◽  
Chromosome 17 ◽  
Mapk Activation ◽  
Age Dependent ◽  
Mitogen Activated Protein ◽  
Activation Status

ABSTRACT Abnormal tau phosphorylation occurs in several neurodegenerative disorders, including Alzheimer's disease (AD) and frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17). Here, we compare mechanisms of tau phosphorylation in mouse models of FTDP-17 and AD. Mice expressing a mutated form of human tau associated with FTDP-17 (tauV337M) showed age-related increases in exogenous tau phosphorylation in the absence of increased activation status of a number of kinases known to phosphorylate tau in vitro. In a “combined” model, expressing both tauV337M and the familial amyloid precursor protein AD mutation APPV717I in a CT100 fragment, age-dependent tau phosphorylation occurred at the same sites and was significantly augmented compared to “single” tauV337M mice. These effects were concomitant with increased activation status of mitogen-activated protein kinase (MAPK) family members (extracellular regulated kinases 1 and 2, p38, and c-Jun NH2-terminal kinase) but not glycogen synthase kinase-3αβ or cyclin-dependent kinase 5. The increase in MAPK activation was a discrete effect of APPV717I-CT100 transgene expression as near identical changes were observed in single APPV717I-CT100 mice. Age-dependent deficits in memory were also associated with tauV337M and APPV717I-CT100 expression. The data reveal distinct routes to abnormal tau phosphorylation in models of AD and FTDP-17 and suggest that in AD, tau irregularities may be linked to processing of APP C-terminal fragments via specific effects on MAPK activation status.

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